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B3DVG5

- RBL_METI4

UniProt

B3DVG5 - RBL_METI4

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL, rbcL, Minf_1264
Organism
Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum (strain V4))
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site By similarity.UniRule annotation

Catalytic activityi

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.UniRule annotation
3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.UniRule annotation

Cofactori

Binds 1 magnesium ion per subunit By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei126 – 1261Substrate; in homodimeric partner By similarity
Binding sitei176 – 1761Substrate By similarity
Active sitei178 – 1781Proton acceptor By similarity
Binding sitei180 – 1801Substrate By similarity
Metal bindingi204 – 2041Magnesium; via carbamate group By similarity
Metal bindingi206 – 2061Magnesium By similarity
Metal bindingi207 – 2071Magnesium By similarity
Active sitei296 – 2961Proton acceptor By similarity
Binding sitei297 – 2971Substrate By similarity
Binding sitei329 – 3291Substrate By similarity
Sitei336 – 3361Transition state stabilizer By similarity
Binding sitei381 – 3811Substrate By similarity

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. monooxygenase activity Source: UniProtKB-KW
  3. ribulose-bisphosphate carboxylase activity Source: UniProtKB-HAMAP
Complete GO annotation...

GO - Biological processi

  1. reductive pentose-phosphate cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMINF481448:GJEI-1289-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chain (EC:4.1.1.39)
Short name:
RuBisCO large subunit
Gene namesi
Name:cbbL
Synonyms:rbcL
Ordered Locus Names:Minf_1264
OrganismiMethylacidiphilum infernorum (isolate V4) (Methylokorus infernorum (strain V4))
Taxonomic identifieri481448 [NCBI]
Taxonomic lineageiBacteriaVerrucomicrobiaunclassified VerrucomicrobiaMethylacidiphilalesMethylacidiphilaceaeMethylacidiphilum
ProteomesiUP000009149: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 486486Ribulose bisphosphate carboxylase large chainUniRule annotation
PRO_0000355750Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei204 – 2041N6-carboxylysine By similarity

Proteomic databases

PRIDEiB3DVG5.

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains By similarity.

Protein-protein interaction databases

STRINGi481448.Minf_1264.

Structurei

3D structure databases

ProteinModelPortaliB3DVG5.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiCTPLKQA.
OrthoDBiEOG6ZKXMS.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1.
InterProiIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEiPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B3DVG5-1 [UniParc]FASTAAdd to Basket

« Hide

MVIAGDGKAG AKKSRWSAGV TPYAEMGYYN ADYVPKDTDI LAAFRFVPQE    50
GVEPIEAGAA VAGESSTATW TVVWTDRLTA YEHYQGKCFR VEPVPGTNQY 100
IAFIAYDLDL FEEGSIANMS SSIIGNVFGF KALKSLRLED LRIPPHYVKT 150
FQGPAHGIMM EREYLNKYGR PLLGATVKPK LGLSAKNYGR VVYEALRGGL 200
DFTKDDENIN SQPFMRWRDR WLFCMEAVNK AMAETGEIKG HYLNVTAATM 250
EEMYERAEFA KELGSVIIMV DLTAGFTAIQ SMAKWCRKNG VLLHLHRAGH 300
STYTRQKIHG VNFRVIAKWM RLAGVDHIHA GTVVGKLEGD LHSVQGYYKT 350
LRTQYTEADP LLGLYFEQDW ASMPGVMPVA SGGIHAGQMH LLLSYLGEDT 400
ILQFGGGTIG HPDGIAAGAT ANRVAVEVMV QARNEGKDIL REGPEILEKA 450
CRWSPALAKA IETWKDISFE FESTDVPDAV AMPTIA 486
Length:486
Mass (Da):53,694
Last modified:July 22, 2008 - v1
Checksum:iA0A9CE650CA08146
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000975 Genomic DNA. Translation: ACD83318.1.
RefSeqiYP_001939916.1. NC_010794.1.

Genome annotation databases

EnsemblBacteriaiACD83318; ACD83318; Minf_1264.
GeneIDi6352199.
KEGGimin:Minf_1264.
PATRICi22491667. VBIMetInf111569_1320.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000975 Genomic DNA. Translation: ACD83318.1 .
RefSeqi YP_001939916.1. NC_010794.1.

3D structure databases

ProteinModelPortali B3DVG5.
ModBasei Search...

Protein-protein interaction databases

STRINGi 481448.Minf_1264.

Proteomic databases

PRIDEi B3DVG5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACD83318 ; ACD83318 ; Minf_1264 .
GeneIDi 6352199.
KEGGi min:Minf_1264.
PATRICi 22491667. VBIMetInf111569_1320.

Phylogenomic databases

eggNOGi COG1850.
HOGENOMi HOG000230831.
KOi K01601.
OMAi CTPLKQA.
OrthoDBi EOG6ZKXMS.

Enzyme and pathway databases

BioCyci MINF481448:GJEI-1289-MONOMER.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPi MF_01338. RuBisCO_L_type1.
InterProi IPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view ]
Pfami PF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view ]
SUPFAMi SSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEi PS00157. RUBISCO_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete genome sequence of the extremely acidophilic methanotroph isolate V4, Methylacidiphilum infernorum, a representative of the bacterial phylum Verrucomicrobia."
    Hou S., Makarova K.S., Saw J.H., Senin P., Ly B.V., Zhou Z., Ren Y., Wang J., Galperin M.Y., Omelchenko M.V., Wolf Y.I., Yutin N., Koonin E.V., Stott M.B., Mountain B.W., Crowe M.A., Smirnova A.V., Dunfield P.F.
    , Feng L., Wang L., Alam M.
    Biol. Direct 3:26-26(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Isolate V4.

Entry informationi

Entry nameiRBL_METI4
AccessioniPrimary (citable) accession number: B3DVG5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: July 22, 2008
Last modified: May 14, 2014
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric "cap" on each end of the "barrel" By similarity.

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi